|Application ||WB, E|
|Other Accession||P26233, Q9WU82, Q02248, Q0VCX4, P18824, NP_001091679.1|
|Predicted||Drosophila, Bovine, Mouse, Rat, Xenopus|
|Calculated MW||85497 Da|
|Antigen Region||646-673 aa|
|Other Names||Catenin beta-1, Beta-catenin, CTNNB1, CTNNB|
|Target/Specificity||This CTNNB1 antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 646-673 amino acids from human CTNNB1.|
|Format||Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CTNNB1 Antibody (Ascites) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell junction. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1 Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells.|
|Tissue Location||Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is part of a complex of proteins that constitute adherens junctions (AJs). AJs are necessary for the creation and maintenance of epithelial cell layers by regulating cell growth and adhesion between cells. The encoded protein also anchors the actin cytoskeleton and may be responsible for transmitting the contact inhibition signal that causes cells to stop dividing once the epithelial sheet is complete. Finally, this protein binds to the product of the APC gene, which is mutated in adenomatous polyposis of the colon. Mutations in this gene are a cause of colorectal cancer (CRC), pilomatrixoma (PTR), medulloblastoma (MDB), and ovarian cancer. Three transcript variants encoding the same protein have been found for this gene.
Huang, W., et al. Mol. Cell. Biol. 30(19):4575-4594(2010)
Chairoungdua, A., et al. J. Cell Biol. 190(6):1079-1091(2010)
Mirza, M.K., et al. J. Exp. Med. 207(8):1675-1685(2010)
Guo, Q., et al. Acta Biochim. Biophys. Sin. (Shanghai) 42(7):450-456(2010)
Teng, Y., et al. Zhonghua Yi Xue Za Zhi 90(14):988-992(2010)
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